β-Catenin/Tcf-regulated transcription prior to the midblastula transition

Yang, Jing; Tan, Change; Darken, Rachel S.; Wilson, P. David; Klein, Peter S.

doi:10.1242/dev.00150

Cited by 198 publications

(173 citation statements)

References 43 publications

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“…Instead, maternal JNK has an unusual pattern of temporal activity that starts from oocyte maturation and ends at early gastrulation, coinciding with the formation of dorsal structures. Thus, although a confined and low level of nuclear ␤-catenin specifies the future dorsal axis in early Xenopus embryos (37), the sustained high level of maternal JNK activity may act as a gatekeeper to prevent promiscuous nuclear ␤-catenin accumulation that could lead to hyperdorsalization. Taken together, these results suggest that Ca 2ϩ ͞CamKII͞NFAT and Dsh͞JNK provide spatial and temporal regulation of the canonical Wnt signaling, respectively, for axis formation in Xenopus embryos.…”

Section: Discussionmentioning

confidence: 99%

Jun NH ₂ -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos

Liao

Tao

Kofron

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Jun NH2-terminal kinases (JNKs) regulate convergent extension movements in Xenopus embryos through the noncanonical Wnt͞ planar cell polarity pathway. In addition, there is a high level of maternal JNK activity spanning from oocyte maturation until the onset of gastrulation that has no defined functions. Here, we show that maternal JNK activation requires Dishevelled and JNK is enriched in the nucleus of Xenopus embryos. Although JNK activity is not required for the glycogen synthase kinase-3-mediated degradation of ␤-catenin, inhibition of the maternal JNK signaling by morpholino-antisense oligos causes hyperdorsalization of Xenopus embryos and ectopic expression of the Wnt͞␤-catenin target genes. These effects are associated with an increased level of nuclear and nonmembrane-bound ␤-catenin. Moreover, ventral injection of the constitutive-active Jnk mRNA blocks ␤-catenininduced axis duplication, and dorsal injection of active Jnk mRNA into Xenopus embryos decreases the dorsal marker gene expression. In mammalian cells, activation of JNK signaling reduces Wnt3A-induced and ␤-catenin-mediated gene expression. Furthermore, activation of JNK signaling rapidly induces the nuclear export of ␤-catenin. Taken together, these results suggest that JNK antagonizes the canonical Wnt pathway by regulating the nucleocytoplasmic transport of ␤-catenin rather than its cytoplasmic stability. Thus, the high level of sustained maternal JNK activity in early Xenopus embryos may provide a timing mechanism for controlling the dorsal axis formation. nucelocytoplasmic transport ͉ Wnt

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Section: Discussionmentioning

confidence: 99%

Jun NH ₂ -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos

Liao

Tao

Kofron

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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“…Early zygotic transcription of a gene has been thought to be rare, but examples have been characterized in Xenopus (Yang et al, 2002). Recently, a set of over one hundred zebrafish genes that are transcribed prior to the mid-blastula transition were identified by microarray analysis (Mathavan et al, 2005), although chch was not identified in this screen.…”

Section: Zebrafish Chch Is Expressed Prior To the Mbtmentioning

confidence: 99%

“…Early zygotic transcription of a gene has been thought to be rare, but examples have been characterized in Xenopus (Yang et al, 2002). Recently, a set of over one hundred zebrafish At sphere and shield stages, chch is widely expressed but some cells express higher levels of chch ( fig.…”

Section: Zebrafish Chch Is Expressed Prior To the Mbtmentioning

confidence: 99%

Expression and regulation of the zinc finger transcription factor Churchill during zebrafish development

Londin

Mentzer

Gates

et al. 2007

Gene Expression Patterns

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During gastrulation dynamic cell movements establish the germ layers and shape the body axis of the vertebrate embryo. The zinc finger protein Churchill (chch) has been proposed to be a key regulator of these movements. We examined the expression pattern of chch in zebrafish and studied the regulation of chch by FGF signaling. We observed zygotic expression of chch during early cleavage stages. Two lines of evidence demonstrate that chch is zygotically expressed prior to the mid-blastula transition. First, blocking transcription during early cleavage stages represses chch expression. Second, endogenous levels of chch transcripts increase between 1-cell and 16-cell embryos. chch remains widely expressed during blastula and gastrula stages but scattered cells express higher levels of chch. By somitogenesis, chch is expressed in the ventral-most cells of the embryo adjacent to the yolk. In addition, transcripts are also observed in superficial cells on the surface of the yolk, in presumptive mucous cells and keratinocytes. By 30 hpf transcripts are observed in anterior neural tissue and ventral cells adjacent to the yolk. Over the next three days chch expression is indistinct until 4 dpf when we observe expression in the pharynx and gut. We show that activation of FGF signaling during gastrulation is sufficient to induce chch expression. In addition, we demonstrate that blocking FGF signaling between the 4-cell and shield stages represses chch expression. Results and DiscussionChurchill (chch) is a small, highly conserved zinc finger transcription factor identified in a differential screen to isolate genes induced by Hensen's node (Sheng et al., 2003). chch was proposed to function as a switch between the functions of FGF in neural and mesoderm induction (Sheng et al., 2003). Morpholino knockdown of chch in the chick epiblast results in inappropriate migration of cells through the primitive streak (Sheng et al., 2003). This demonstrates that chch represses the movement of epiblast cells and allows them to remain in the prospective neural plate where they subsequently give rise to neural tissue (Sheng et al., 2003). Overexpression of chch in Xenopus embryos results in suppression of the mesodermal marker brachyury (Xbra) in embryos and animal cap assays (Sheng et al., 2003;Snir et al., 2006). FGF4 or FGF8 are sufficient to induce chch expression in the chick. In Xenopus, chch expression is regulated by XLPOU91 which mediates FGF responsiveness (Snir et al., 2006 Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. (Sheng et al., 2003;Snir et al., 2006). Sip1 is a direct r...

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“…However, no difference of the E2F mobility during development seems to preclude this hypothesis. Thirdly, basic transcriptional machinery may be activated at or around MBT, which seems most feasible, but a recent report suggests that some transcription of mRNA from zygotic genome before MBT was active (Yang et al, 2002), although the detailed analysis remains to be done.…”

Section: Discussionmentioning

confidence: 99%

Dominant Negative E2F Inhibits Progression of the Cell Cycle after the Midblastula Transition in Xenopus

Tanaka

Ono

Kitamura

et al. 2003

Cell Struct. Funct.

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ABSTRACT. The cleavage cycle, which is initiated by fertilization, consists of only S and M phases, and the gap phases (G1 and G2) appear after the midblastula transition (MBT) in the African clawed frog, Xenopus laevis. During early development in Xenopus, we examined the E2F activity, which controls transition from the G1 to S phase in the somatic cell cycle. Gel retardation and transactivation assays revealed that, although the E2F protein was constantly present throughout early development, the E2F transactivation activity was induced in a stagespecific manner, that is, low before MBT and rapidly increased after MBT. Introduction of the recombinant dominant negative E2F (dnE2F), but not the control, protein into the 2-cell stage embryos specifically suppressed E2F activation after MBT. Cells in dnE2F-injected embryos appeared normal before MBT, but ceased to proliferate and eventually died at the gastrula. These cells contained decreased cdk activity with enhanced inhibitory phosphorylation of Cdc2 at Tyr15. Thus, E2F activity is required for cell cycle progression and cell viability after MBT, but not essential for MBT transition and developmental progression during the cleavage stage.

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β-Catenin/Tcf-regulated transcription prior to the midblastula transition

Cited by 198 publications

References 43 publications

Jun NH ₂ -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos

Jun NH ₂ -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos

Expression and regulation of the zinc finger transcription factor Churchill during zebrafish development

Dominant Negative E2F Inhibits Progression of the Cell Cycle after the Midblastula Transition in Xenopus

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β-Catenin/Tcf-regulated transcription prior to the midblastula transition

Cited by 198 publications

References 43 publications

Jun NH 2 -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos

Jun NH 2 -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos

Expression and regulation of the zinc finger transcription factor Churchill during zebrafish development

Dominant Negative E2F Inhibits Progression of the Cell Cycle after the Midblastula Transition in Xenopus

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Product

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Jun NH ₂ -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos

Jun NH ₂ -terminal kinase (JNK) prevents nuclear β-catenin accumulation and regulates axis formation in Xenopus embryos